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Open data
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Basic information
| Entry | Database: PDB / ID: 8qjr | ||||||
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| Title | BRG1 bromodomain in complex with VBC via compound 17 | ||||||
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Keywords | GENE REGULATION / BRG1 / BROMODOMAIN / VHL / ELONGIN / VBC / E3 LIGASE / VON HIPPEL-LINDAU / UBIQUITINASE | ||||||
| Function / homology | Function and homology informationpositive regulation of glucose mediated signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / regulation of cellular response to hypoxia / neural retina development / npBAF complex / nBAF complex / negative regulation of androgen receptor signaling pathway / EGR2 and SOX10-mediated initiation of Schwann cell myelination / nucleosome array spacer activity ...positive regulation of glucose mediated signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / regulation of cellular response to hypoxia / neural retina development / npBAF complex / nBAF complex / negative regulation of androgen receptor signaling pathway / EGR2 and SOX10-mediated initiation of Schwann cell myelination / nucleosome array spacer activity / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / GBAF complex / regulation of G0 to G1 transition / Tat protein binding / transcription elongation factor activity / target-directed miRNA degradation / RNA polymerase I preinitiation complex assembly / elongin complex / RSC-type complex / ATP-dependent chromatin remodeler activity / regulation of nucleotide-excision repair / host-mediated activation of viral transcription / Replication of the SARS-CoV-1 genome / nucleosome disassembly / VCB complex / Cul5-RING ubiquitin ligase complex / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Cul2-RING ubiquitin ligase complex / positive regulation of T cell differentiation / intracellular membraneless organelle / nuclear androgen receptor binding / positive regulation of double-strand break repair / SUMOylation of ubiquitinylation proteins / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of G1/S transition of mitotic cell cycle / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / negative regulation of transcription elongation by RNA polymerase II / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / positive regulation of signal transduction by p53 class mediator / negative regulation of cell differentiation / positive regulation of Wnt signaling pathway / ATP-dependent activity, acting on DNA / positive regulation of myoblast differentiation / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Chromatin modifying enzymes / Formation of RNA Pol II elongation complex / DNA polymerase binding / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / Interleukin-7 signaling / transcription initiation-coupled chromatin remodeling / negative regulation of autophagy / protein serine/threonine kinase binding / transcription corepressor binding / transcription coregulator binding / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / positive regulation of cell differentiation / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Formation of the beta-catenin:TCF transactivating complex / helicase activity / negative regulation of cell growth / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / kinetochore / positive regulation of miRNA transcription / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Regulation of expression of SLITs and ROBOs / RMTs methylate histone arginines / nuclear matrix / fibrillar center / cell morphogenesis / ubiquitin-protein transferase activity / p53 binding / transcription corepressor activity / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / nervous system development / positive regulation of cold-induced thermogenesis / Neddylation / microtubule cytoskeleton / regulation of gene expression / protein-containing complex assembly / Replication of the SARS-CoV-2 genome / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.17 Å | ||||||
Authors | Kerry, P.S. / Hole, A.J. / Perez-Dorado, J.I. | ||||||
| Funding support | 1items
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Citation | Journal: J.Med.Chem. / Year: 2024Title: PROTACs Targeting BRM (SMARCA2) Afford Selective In Vivo Degradation over BRG1 (SMARCA4) and Are Active in BRG1 Mutant Xenograft Tumor Models. Authors: Berlin, M. / Cantley, J. / Bookbinder, M. / Bortolon, E. / Broccatelli, F. / Cadelina, G. / Chan, E.W. / Chen, H. / Chen, X. / Cheng, Y. / Cheung, T.K. / Davenport, K. / DiNicola, D. / ...Authors: Berlin, M. / Cantley, J. / Bookbinder, M. / Bortolon, E. / Broccatelli, F. / Cadelina, G. / Chan, E.W. / Chen, H. / Chen, X. / Cheng, Y. / Cheung, T.K. / Davenport, K. / DiNicola, D. / Gordon, D. / Hamman, B.D. / Harbin, A. / Haskell, R. / He, M. / Hole, A.J. / Januario, T. / Kerry, P.S. / Koenig, S.G. / Li, L. / Merchant, M. / Perez-Dorado, I. / Pizzano, J. / Quinn, C. / Rose, C.M. / Rousseau, E. / Soto, L. / Staben, L.R. / Sun, H. / Tian, Q. / Wang, J. / Wang, W. / Ye, C.S. / Ye, X. / Zhang, P. / Zhou, Y. / Yauch, R. / Dragovich, P.S. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8qjr.cif.gz | 387.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8qjr.ent.gz | 318.4 KB | Display | PDB format |
| PDBx/mmJSON format | 8qjr.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8qjr_validation.pdf.gz | 924.6 KB | Display | wwPDB validaton report |
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| Full document | 8qjr_full_validation.pdf.gz | 937.8 KB | Display | |
| Data in XML | 8qjr_validation.xml.gz | 34 KB | Display | |
| Data in CIF | 8qjr_validation.cif.gz | 46.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qj/8qjr ftp://data.pdbj.org/pub/pdb/validation_reports/qj/8qjr | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8qjsC ![]() 8qjtC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-Protein , 4 types, 8 molecules ADBECFGH
| #1: Protein | Mass: 11748.406 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: ![]() #2: Protein | Mass: 10974.616 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Production host: ![]() #3: Protein | Mass: 18702.291 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Production host: ![]() #4: Protein | Mass: 14230.447 Da / Num. of mol.: 2 / Fragment: UNP residues 1418-1536 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA4, BAF190A, BRG1, SNF2B, SNF2L4 / Production host: ![]() References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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-Non-polymers , 5 types, 68 molecules 








| #5: Chemical | ChemComp-PO4 / #6: Chemical | ChemComp-GOL / | #7: Chemical | #8: Chemical | ChemComp-CL / | #9: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.61 % |
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / Details: 27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å |
| Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 24, 2020 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 3.17→80.64 Å / Num. obs: 20137 / % possible obs: 98.9 % / Redundancy: 3.6 % / CC1/2: 0.984 / Rmerge(I) obs: 0.15 / Net I/σ(I): 6.3 |
| Reflection shell | Resolution: 3.17→3.39 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.578 / Mean I/σ(I) obs: 2 / Num. unique obs: 3675 / CC1/2: 0.755 / % possible all: 99.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.17→80.64 Å / Cor.coef. Fo:Fc: 0.865 / Cor.coef. Fo:Fc free: 0.862 / Cross valid method: THROUGHOUT / SU Rfree Blow DPI: 0.523
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| Displacement parameters | Biso mean: 67.49 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.51 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.17→80.64 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 3.17→3.19 Å
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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Homo sapiens (human)
X-RAY DIFFRACTION
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